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The tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is apromising candidate for cancer therapeutics that exhibits the ability to preferentiallyinduce apoptosis in malignant cells. RGD peptides bind to the integrins, ανβ3and ανβ5, which are selectively expressed in tumor neovasculature and at the surfaceof certain tumor cells. To enhance the antitumor effect, an RGD-TRAIL protein,in which TRAIL was fused with the RGD motif-containing cell adhesive sequence,GRGDNP (gly-arg-gly-asp-asn-pro), was constructed and evaluated for bioactivity.The soluble TRAIL and RGD-TRAIL proteins were expressed in Escherichia coli BL21(DE3) and purified using a non-denaturing method. The antitumor effect of thepurified RGD-TRAIL on cell proliferation was evaluated in vitro using MTT andwound healing assays and cell apoptosis was assessed by Hoechst 33342 stainingand PARP expression analysis. The results revealed that RGD-TRAIL inhibited theproliferation of multiple tumor cell lines (A549, NCI-H1299 and HCC827). Westernblot analysis demonstrated that the treatment of tumor cells with RGD-TRAIL activatedthe apoptotic pathway by the cleavage of PARP, in the same way as wild-type TRAIL(wtTRAIL). These results demonstrate that RGD-TRAIL possesses more potent antitumoreffects than wtTRAIL and, therefore, merits further investigation in preclinicaland clinical studies.

Induction of non-small cell lung carcinoma apoptosis using soluble RGD-TRAIL by targeting the integrin receptor of tumor cells